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• W2040803819 abstract "Histone H3 phosphorylation is a critical step that couples signal transduction pathways to gene regulation. To specifically assess the transcriptional regulatory functions of H3 phosphorylation, we developed an in vivo targeting approach and found that the H3 kinase MSK1 is a direct and potent transcriptional activator. Targeting of this H3 kinase to the endogenous c-fos promoter is sufficient to activate its expression without the need of upstream signaling. Moreover, targeting MSK1 to the α-globin promoter induces H3 S28 phosphorylation and reactivates expression of this polycomb-silenced gene. Importantly, we discovered a mechanism whereby H3 S28 phosphorylation not only displaces binding of the polycomb-repressive complexes, but it also induces a methyl-acetylation switch of the adjacent K27 residue. Our findings show that signal transduction activation can directly regulate polycomb silencing through a specific histone code-mediated mechanism." @default.
• W2040803819 created "2016-06-24" @default.
• W2040803819 creator A5018318563 @default.
• W2040803819 creator A5037375363 @default.
• W2040803819 date "2011-01-31" @default.
• W2040803819 modified "2023-10-11" @default.
• W2040803819 title "Histone code pathway involving H3 S28 phosphorylation and K27 acetylation activates transcription and antagonizes polycomb silencing" @default.
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• W2040803819 doi "https://doi.org/10.1073/pnas.1012798108" @default.
• W2040803819 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3041124" @default.
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